A recombinant full-length human protein was used as the immunogen for the MTF1 antibody.
The metal-responsive element (MRE)-binding transcription factor (MTF-1) stimulates the expression of metallothioneins in response to the exposure of cells to heavy metals. MTF-1 contains six zinc fingers in the DNA binding domain. The phosphorylation of MTF-1 in response to metal exposure appears to play a significant role in the ability of MTF-1 to activate metallothionein transcription. In addition to its role in metallothionein activation, MTF-1 is involved in a post-transcription regulatory complex for ribosomal protein S25. MTF-1, La and p53 inhibit the nuclear export of S25 mRNA in response to nutrient depravation. Furthermore, MTF-1 acts as a chromatin insulator on integrated transgenes in cultured cells to insulate active loci against chromatin silencing.
